Biological Compounds Flashcards

wk 3

1
Q

What is the most important carbohydrate?

A

Glucose- transports energy

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2
Q

What are the four biological compounds?

A

carbohydrates, proteins, fats and nucleic acids

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3
Q

What are the different types of fats?

A

fats, oils, phospholipids, steroids and modified fatty acids.

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4
Q

What are the 4 categories of carbohydrates?

A

monosaccharides, disaccharides, oligosaccharides and polysaccharides

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5
Q

What is the structure of monosaccharides?

A

3 or more carbon atoms where a carbonyl group is bonded to the first carbon

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6
Q

What are examples of monosaccharides?

A

glucose. ribose and fructose

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7
Q

What way does an alpha glucose face?

A

down - OH on bottom

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8
Q

what way does beta glucose face?

A

up- OH on top

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9
Q

Describe what is meant by the 1,2 glycosidic linkage of maltose.

A

OH of Carbon 1 reacts/bonds with Caron 4 of other d-glucose.

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10
Q

What are disaccharides and an example.

A

2 monosaccharides linked by covalent bonds. E.g. Sucrose (glucose and fructose)

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11
Q

what are Oligosaccharides?

A

several monosaccharides bound by glycosidic linkages.

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12
Q

What is an example of an oligosaccharide?

A

Starch

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13
Q

what are polysaccharides

A

polymers made up of hundreds and thousands of monosaccharides.

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14
Q

Describe the structure of polysaccharides.

A

Can be branched which will limit no. of H-bonds (starch and glycogen) or unbranched which are chemically stable (cellulose)

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15
Q

If you have a polysaccharide of all alpha glucose how will they be drawn/ orientated?

A

all the SAME way

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16
Q

If you have a polysaccharide of all beta glucose how will they be drawn/ orientated?

A

Alternating

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17
Q

What type of reaction bonds monosaccharides to create the others?

A

condesation reactions

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18
Q

What are the characteristics of hydrocarbons

A

insoluble in water, many covalent bonds.

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19
Q

How are triglycerides made?

A

Glycerol and a fatty acid creating an ester linkage

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20
Q

describe saturated fats

A

No double bonds allowing them to be tightly packed

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21
Q

describe unsaturated fats

A

double bonds creating a kink in the carbon chain

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22
Q

what do phosplipids create that are important to cells?

A

the lipid bilayer. Phosphate + choline = head and fatty acid forms the chain.

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23
Q

differentiate between DNA and RNA

A

DNA sequence carries information that RNA uses to create protein structure.

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24
Q

how many H bonds are there between A and T?

A

two

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25
Which DNA bases are pyrimidine?
Cytosine and thymine
26
what type of bond joins strands together and what are they made up of?
Phosphodiester bonds- between sugar and phosphate
27
what is the structure of an amino acid?
carboxyl and amino functinal group with a R (side chain)
28
What is the most common isomeric form of amino acids?
L
29
Describe the peptide linkage that builds amino acid that bonds two amino acids
carboxyl of one amino acids undergoes condensation reaction with amino group of the other.
30
what are the six non-polar and aliphatic amino acids?
Glycine, alanine, proline, valine, leucine and isoleucine
31
what are the three aromatic ring structure amino acids and their polarity?
Phe (non-polar), tyr (polar) and trp (polar)
32
what are the two sulfur containing amino acids?
methionine and cystine
33
what is primary structure?
order of the amino acid
34
what are the two forms of secondary structure
Alpha helix (right handed coil) and beta pleated sheets (2 or more peptide chains aligned)
35
what is tertiary structure?
bending and folding to create a 3D shape. Creates an outer surface for the subunits to interact with
36
Quaternary Structure
Subunits interact via hydrophobic interactions
37
what are the functions of polysaccharides?
store energy and provide structural materials
38
what is the function of fats and oils?
energy storage
39
what is the function of phospholipids?
structural, communication
40
what are the functions of DNA and RNA (nucleic acid)
replication, transcription and translation.
41
what are the types of proteins?
Enzymes, hormonal and regulatory, receptors, storage, structural, transport and genetic regulatory proteins
42
what is an example of defensive protein, receptor protein and transport protein respectively?
antobodies, insulin receptors and haemoglobin.
43
What is cellulose made up of?
UNBRANCHED chains of glucose molecules linked by beta 1,4 glycosidic bonds
44
What are the glycosidic bonds of Starch?
alpha 1,6 and alpha 1,4 linkage
45
what is the glycosidic bond of sucrose?
alpha 1,2
46
What is the glycosidic bond of maltose?
alpha 1,4 linkage
47
What two monosaccharides make up maltose?
alpha and beta glucose
48
what two monosaccharides make up lactose?
galactose and glucose
49
what two monosaccharides make up sucrose?
fructose and glucose
50
Describe properties of Secondary structure.
It is important to have ability for peptide bonds to form H bonds, the steric influence of amino acid residues and the hydrophobic/philic character.
51
Order to which amino acids are linked together in a protein =
primary structure
52
regions of ordered structure =
secondary structure
53
What is the strongest form of intermolecular (between atoms) formed involving amino acid serine?
hydrogen bond
54
what is DNA made of?
nucleotide monophosphates
55
What is a Heterodimeric Protein?
two protein subunits that differ from each other
56
What are fats, lipids and steroids made up of in the body?
lipids
57
What is the role of polarity in protein structure?
polar= charged and hydrophilic, non-polar= uncharged and hydrophobic, H-bonds strongest and proved stability
58
How do amino acids mainatin stability in proteins?
Form covalent bond linkages that bind the peptides together.
59
Give four examples of lipids.
In vitiman A, phospholipids, triglcerols and steroids
60
How is glucose stored in the body?
in glycogen
61
How are fats transported around the body?
in lipoproteins